Heterogeneity of the S-100 protein specific binding sites in synaptosomal particulate fractions and subfractions.
The specific interaction of S-100 protein with synaptosomal particulate fractions (SYN) was further investigated with special reference to the number of binding components and their localization in synaptosomal subfractions. Binding studies were conducted on SYN from various CNS regions, on synaptosomal subfractions from the cerebral cortex, and on cerebral cortex SYN under various conditions. The results suggest that S-100 binds to two populations of membrane sites: high -affinity sites, which seem to be confined to neuronal membranes (synaptosomal plasma membranes and synaptic vesicles), and low-affinity sites, which are also detected in other membranes. The data are consistent with the view that the biphasic profile of S-100 binding to SYN does not result from heterogeneity of the S-100 molecule, and that the Ca2+ conformation of the protein is as important as the proper conformation of the binding site for full expression of high-affinity binding.
D000818:Animals; D001665:Binding Sites / Q000187:drug effects; D001921:Brain / Q000378:metabolism*; D002540:Cerebral Cortex / Q000378:metabolism; D004492:Edetic Acid / Q000494:pharmacology; D005260:Female; D008297:Male; D009419:Nerve Tissue Proteins / Q000378:metabolism*; D010739:Phospholipase D / Q000494:pharmacology; D011189:Potassium Chloride / Q000494:pharmacology; D011485:Protein Binding; D051381:Rats; D011919:Rats, Inbred Strains; D009418:S100 Proteins / Q000378:metabolism*; D013570:Synaptic Membranes / Q000378:metabolism*; D010738:Type C Phospholipases / Q000494:pharmacology
D009419:Nerve Tissue Proteins; D009418:S100 Proteins; D011189:Potassium Chloride; D004492:Edetic Acid; D010738:Type C Phospholipases; D010739:Phospholipase D